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    "title": "Why your protein condensates age into amyloid faster than",
    "entity": "Why your protein condensates age into amyloid faster than",
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    "tldr": "hnRNPA2B1 mutations in the C-terminal domain accelerate the transition of liquid protein droplets into solid, amyloid-like fibrils. Here's how condensates age.",
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            "entity": "Why your protein condensates age into amyloid faster than",
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            "value": "Why your protein condensates age into amyloid faster than",
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            "value": "2026-08-29",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
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            "entity": "Why your protein condensates age into amyloid faster than",
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            "value": "PreppinPeppers Editorial Team",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
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            "value": "peptide research, Research, study",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
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            "category": "content",
            "entity": "Why your protein condensates age into amyloid faster than",
            "attribute": "summary",
            "value": "hnRNPA2B1 mutations in the C-terminal domain accelerate the transition of liquid protein droplets into solid, amyloid-like fibrils. Here's how condensates age.",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
            "evidence": "https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than"
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            "id": "why-your-protein-condensates-age-into-amyloid-faster-than:section-1",
            "category": "content",
            "entity": "Why your protein condensates age into amyloid faster than",
            "attribute": "section",
            "value": "What hnRNPA2B1 is",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
            "evidence": "https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than"
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            "category": "content",
            "entity": "Why your protein condensates age into amyloid faster than",
            "attribute": "section",
            "value": "What hnRNPA2B1 actually is, and why the droplets matter",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
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            "entity": "Why your protein condensates age into amyloid faster than",
            "attribute": "section",
            "value": "The key finding: mutations accelerate condensate maturation",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
            "evidence": "https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than"
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            "value": "Why this matters beyond neurodegeneration",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
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            "value": "Practical bench notes for LLPS-prone peptide and protein reagents",
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            "value": "this coverage at bioRxiv → - www.biorxiv.org",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
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            "value": "Xu et al., J Biol Chem 2022: Manganese promotes α-synuclein amyloid aggregation through the induction of protein phase transition - pmc.ncbi.nlm.nih.gov",
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            "value": "Liu et al., Adv Sci (Weinh) 2026: Protein Disulfide Isomerase Disassembles TDP-43/G3BP1 Condensates and Antagonizes TDP-43 Pathological Aggregates - pmc.ncbi.nlm.nih.gov",
            "source": "Lab article (https://www.preppinpeppers.com/blogs/the-lab/why-your-protein-condensates-age-into-amyloid-faster-than)",
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    "faq": [
        {
            "q": "What is hnRNPA2B1 and why do its droplets matter?",
            "a": "It is an RNA-binding protein whose low-complexity domain drives liquid–liquid phase separation to form membraneless organelles. The same self-association can misfire into solid aggregates, which is why its droplets are a focal point in neurodegeneration research."
        },
        {
            "q": "How do the D302V and P310L mutations change condensate behavior?",
            "a": "They make condensates form faster, fuse less freely, and harden into amyloid-positive cores. Fibrils emerge directly from the droplet interior rather than from bulk solution, showing the condensate itself is the aggregation intermediate."
        },
        {
            "q": "Can a short peptide fragment really drive aggregation of the full protein?",
            "a": "Yes. A conserved 25-amino-acid LCD region containing both mutation sites is sufficient to form amyloid fibrils on its own and to seed aggregation of the full LCD when added to pre-formed droplets, even though it cannot phase separate by itself."
        }
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                        "text": "It is an RNA-binding protein whose low-complexity domain drives liquid–liquid phase separation to form membraneless organelles. The same self-association can misfire into solid aggregates, which is why its droplets are a focal point in neurodegeneration research."
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                        "text": "Yes. A conserved 25-amino-acid LCD region containing both mutation sites is sufficient to form amyloid fibrils on its own and to seed aggregation of the full LCD when added to pre-formed droplets, even though it cannot phase separate by itself."
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